Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

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RHO Rho (Ras homology) subfamily of Ras-like small GTPases

There are 1103 RHO domains in 1102 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a RHO domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with RHO domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Binding / catalysis: GTP-hydrolysis

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Hall A
  • Rho GTPases and the actin cytoskeleton.
  • Science. 1998; 279: 509-14
  • Display abstract

  • The actin cytoskeleton mediates a variety of essential biological functions in all eukaryotic cells. In addition to providing a structural framework around which cell shape and polarity are defined, its dynamic properties provide the driving force for cells to move and to divide. Understanding the biochemical mechanisms that control the organization of actin is thus a major goal of contemporary cell biology, with implications for health and disease. Members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and furthermore, through their interaction with multiple target proteins, they ensure coordinated control of other cellular activities such as gene transcription and adhesion.

  • Ren XD, Schwartz MA
  • Regulation of inositol lipid kinases by Rho and Rac.
  • Curr Opin Genet Dev. 1998; 8: 63-7
  • Display abstract

  • Rho and Rac small GTPases associate with type-I phosphatidylinositol 4-phosphate 5-kinase to regulate the production of phosphatidylinositol 4,5-bisphosphate. This lipid appears to mediate some of the effects of Rho and Rac on the actin cytoskeleton. The genes for several type-I phosphatidylinositol 4-phosphate 5-kinases have been cloned recently but it is not known which one interacts with Rho and/or Rac. Rho family GTPases also interact with phosphatidylinositol 3-kinase, though this kinase can be either upstream or downstream of the GTPases depending upon the system.

  • Tanaka K, Takai Y
  • Control of reorganization of the actin cytoskeleton by Rho family small GTP-binding proteins in yeast.
  • Curr Opin Cell Biol. 1998; 10: 112-6
  • Display abstract

  • Accumulating evidence indicates that Rho family small GTP-binding proteins regulate reorganization of the actin cytoskeleton. There are members of the Rho family in the budding yeast Saccharomyces cerevisiae, in which powerful molecular genetical approaches are applicable. Recent identification of regulators and targets of the Rho family members has enhanced our understanding of the regulation and modes of action of Rho family members in reorganization of the actin cytoskeleton.

  • Feltham JL et al.
  • Definition of the switch surface in the solution structure of Cdc42Hs.
  • Biochemistry. 1997; 36: 8755-66
  • Display abstract

  • Proteins of the rho subfamily of ras GTPases have been shown to be crucial components of pathways leading to cell growth and the establishment of cell polarity and mobility. Presented here is the solution structure of one such protein, Cdc42Hs, which provides insight into the structural basis for specificity of interactions between this protein and its effector and regulatory proteins. Standard heteronuclear NMR methods were used to assign the protein, and approximately 2100 distance and dihedral angle constraints were used to calculate a set of 20 structures using a combination of distance geometry and simulated annealing refinement. These structures show overall similarity to those of other GTP-binding proteins, with some exceptions. The regions corresponding to switch I and switch II in H-ras are disordered, and no evidence was found for an alpha-helix in switch II. The 13-residue insertion, which is only present in rho-subtype proteins and has been shown to be an important mediator of binding of regulatory and target proteins, forms a compact structure containing a short helix lying adjacent to the beta4-alpha3 loop. The insert forms one edge of a "switch surface" and, unexpectedly, does not change conformation upon activation of the protein by the exchange of GTP analogs for GDP. These studies indicate the insert region forms a stable invariant "footrest" for docking of regulatory and effector proteins.

  • Hirshberg M, Stockley RW, Dodson G, Webb MR
  • The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue.
  • Nat Struct Biol. 1997; 4: 147-52
  • Display abstract

  • The crystal structure of human rac1, a member of the rho family of small G-proteins, complexed with the non-hydrolysable GTP analogue, guanosine-5'-(beta gamma-imino)triphosphate (GMPPNP), has been determined by X-ray analysis at a resolution of 1.38 A. Comparison with the structure of H-ras indicates that rac1 has an extra alpha-helical domain that is characteristic of the rho G proteins, and may be involved in the signalling pathway of this family.

  • Koelle MR
  • A new family of G-protein regulators - the RGS proteins.
  • Curr Opin Cell Biol. 1997; 9: 143-7
  • Display abstract

  • Genetic experiments have recently been used to identify a family of 'regulator of G-protein signaling' (RGS) proteins, which downregulate signaling by heterotrimeric G proteins. The first biochemical studies of RGS proteins have shown that they accelerate the GTPase activities of G-protein alpha subunits, thus driving G proteins into their inactive GDP-bound forms. The physiological significance of the large number of different RGS proteins remains to be explored.

  • Li R, Zhang B, Zheng Y
  • Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190.
  • J Biol Chem. 1997; 272: 32830-5
  • Display abstract

  • The Rho family small GTP-binding proteins are subjected to regulation by Rho GTPase-activating proteins (GAPs) in the course of transmitting diverse intracellular signals. To understand the mechanism of GAP-catalyzed GTP hydrolysis of Rho GTPases, we have studied the interaction between RhoA and p190, the RasGAP binding phosphoprotein which has been implicated as a Rho-specific GAP, by delineating the structural determinants of RhoA and p190 GAP domain (p190GD) that are involved in their functional coupling. Besides the conserved residues Tyr34, Thr37, and Phe39 in the switch I region of RhoA which are required for p190GD interaction, chimeras made between RhoA and Cdc42, a close relative of RhoA with which p190GD interacts 50-fold less efficiently, revealed that residues outside the switch I and neighboring regions of RhoA, residues 85-122 in particular, contain the major p190GD-specifying determinant(s). Mutation of the unique Asp90 of RhoA in this region mostly abolished p190GD stimulation, whereas the corresponding reverse mutation of Cdc42 (S88D) was able to respond to p190GD-catalysis similarly as RhoA. Further kinetic analysis of these mutants provided evidence that Asp90 of RhoA contributes primarily to the specific binding interaction with p190GD. On the other hand, two charged residues of p190GD, Arg1283 and Lys1321, which are located in the putative G-protein binding helix pocket of GAP domain, were found to be involved in different aspects of interaction with RhoA. The R1283L mutant of p190GD lost GAP activity but retained the ability to bind to RhoA, while K1321A failed to stimulate and to bind to RhoA. These results indicate that residue Asp90 constitutes the second GAP-interactive site in RhoA which is mostly responsible for conferring p190GD-specificity, and suggest that the role of p190GD in the GTPase reaction of RhoA is in part to supply active site residue Arg1283 for efficient catalysis.

  • Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ
  • Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.
  • Nature. 1997; 389: 758-62
  • Display abstract

  • Small G proteins of the Rho family, which includes Rho, Rac and Cdc42Hs, regulate phosphorylation pathways that control a range of biological functions including cytoskeleton formation and cell proliferation. They operate as molecular switches, cycling between the biologically active GTP-bound form and the inactive GDP-bound state. Their rate of hydrolysis of GTP to GDP by virtue of their intrinsic GTPase activity is slow, but can be accelerated by up to 10(5)-fold through interaction with rhoGAP, a GTPase-activating protein that stimulates Rho-family proteins. As such, rhoGAP plays a crucial role in regulating Rho-mediated signalling pathways. Here we report the crystal structure of RhoA and rhoGAP complexed with the transition-state analogue GDP.AlF4- at 1.65 A resolution. There is a rotation of 20 degrees between the Rho and rhoGAP proteins in this complex when compared with the ground-state complex Cdc42Hs.GMPPNP/rhoGAP, in which Cdc42Hs is bound to the non-hydrolysable GTP analogue GMPPNP. Consequently, in the transition state complex but not in the ground state, the rhoGAP domain contributes a residue, Arg85(GAP) directly into the active site of the G protein. We propose that this residue acts to stabilize the transition state of the GTPase reaction. RhoGAP also appears to function by stabilizing several regions of RhoA that are important in signalling the hydrolysis of GTP.

  • Rittinger K et al.
  • Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.
  • Nature. 1997; 388: 693-7
  • Display abstract

  • Small G proteins transduce signals from plasma-membrane receptors to control a wide range of cellular functions. These proteins are clustered into distinct families but all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of G proteins, which includes Cdc42Hs, activate effectors involved in the regulation of cytoskeleton formation, cell proliferation and the JNK signalling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GTPase-activating proteins (GAPs) that enhance the rate of GTP hydrolysis by up to 10(5) times. We report here the crystal structure of Cdc42Hs, with the non-hydrolysable GTP analogue GMPPNP, in complex with the GAP domain of p50rhoGAP at 2.7A resolution. In the complex Cdc42Hs interacts, mainly through its switch I and II regions, with a shallow pocket on rhoGAP which is lined with conserved residues. Arg 85 of rhoGAP interacts with the P-loop of Cdc42Hs, but from biochemical data and by analogy with the G-protein subunit G(i alpha1), we propose that it adopts a different conformation during the catalytic cycle which enables it to stabilize the transition state of the GTP-hydrolysis reaction.

  • Scheffzek K et al.
  • The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.
  • Science. 1997; 277: 333-8
  • Display abstract

  • The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.

  • Sprang SR
  • G protein mechanisms: insights from structural analysis.
  • Annu Rev Biochem. 1997; 66: 639-78
  • Display abstract

  • This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins). G proteins include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins. These proteins share a common structural core, exemplified by that of p21ras (Ras), and significant sequence identity, suggesting a common evolutionary origin. Three-dimensional structures of members of the G protein superfamily are considered in light of other biochemical findings about the function of these proteins. Relationships among G protein structures are discussed, and factors contributing to their low intrinsic rate of GTP hydrolysis are considered. Comparison of GTP- and GDP-bound conformations of G proteins reveals how specific contacts between the gamma-phosphate of GTP and the switch II region stabilize potential effector-binding sites and how GTP hydrolysis results in collapse (or reordering) of these surfaces. A GTPase-activating protein probably binds to and stabilizes the conformation of its cognate G protein that recognizes the transition state for hydrolysis, and may insert a catalytic residue into the G protein active site. Inhibitors of nucleotide release, such as the beta gamma subunit of a heterotrimeric G protein, bind selectively to and stabilize the GDP-bound state. Release factors, such as the translation elongation factor, Ts, also recognize the switch regions and destabilize the Mg(2+)-binding site, thereby promoting GDP release. G protein-coupled receptors are expected to operate by a somewhat different mechanism, given that the GDP-bound form of many G protein alpha subunits does not contain bound Mg2+.

  • Sprang SR
  • G proteins, effectors and GAPs: structure and mechanism.
  • Curr Opin Struct Biol. 1997; 7: 849-56
  • Display abstract

  • G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

  • Tesmer JJ, Berman DM, Gilman AG, Sprang SR
  • Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
  • Cell. 1997; 89: 251-61
  • Display abstract

  • RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors.

  • Narumiya S
  • The small GTPase Rho: cellular functions and signal transduction.
  • J Biochem (Tokyo). 1996; 120: 215-28
  • Display abstract

  • Rho, a Ras homologue of small GTPase, is present from yeast to mammals. It shuttles between the active GTP-bound form and the inactive GDP-bound form and works as a switch in stimulus-evoked cell adhesion and motility, enhancement of contractile responses, and cytokinesis. In these actions, Rho directs the reorganization of the actin cytoskeleton at a specific time and at a specific site in the cell. It also activates serum response factor possibly via a kinase cascade and mediates a growth signal to nuclei. Two signalling processes are known to lead to Rho activation: one is activation of certain types of G-protein-coupled receptors such as lysophosphatidic acid receptor, and the other is activation of other small GTPases including Ras, CDC42, and Rac. Molecules catalyzing the GDP-GTP exchange of Rho, Rho guanine nucleotide exchange factors (Rho GEF), and those catalyzing the acceleration of GTP hydrolysis, Rho GTPase activating proteins (Rho GAP), were identified as Dbl- and Bcr-containing molecules, respectively. In addition, a molecule inhibiting guanine nucleotide exchange of Rho, Rho guanine nucleotide dissociation inhibitor (Rho-GDI), was isolated and characterized. More recently, putative Rho targets possibly mediating various Rho actions have been identified by their selective interaction with GTP-bound Rho. They include lipid kinases such as phosphatidyl-inositol-5-kinase and protein serine/threonine kinases such as PKN and p160ROCK. A model of the molecular mechanism of action of Rho constructed on the basis of these findings is presented. There are, however, still many unclarified links between cell stimulation, Rho activation and final Rho actions.

  • Scheffzek K, Lautwein A, Kabsch W, Ahmadian MR, Wittinghofer A
  • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.
  • Nature. 1996; 384: 591-6
  • Display abstract

  • Ras-related GTP-binding proteins function as molecular switches which cycle between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common timing mechanism that mediates the return from the 'on' to the 'off'-state. It is usually slow but can be accelerated by orders of magnitude upon interaction with GTPase-activating proteins (GAPs). In the case of Ras, a major regulator of cellular growth, point mutations are found in approximately 30% of human tumours which render the protein unable to hydrolyse GTP, even in the presence of Ras-GAPs. The first structure determination of a GTPase-activating protein reveals the catalytically active fragment of the Ras-specific p120GAP (ref. 2), GAP-334, as an elongated, exclusively helical protein which appears to represent a novel protein fold. The molecule consists of two domains, one of which contains all the residues conserved among different GAPs for Ras. From the location of conserved residues around a shallow groove in the central domain we can identify the site of interaction with Ras x GTP. This leads to a model for the interaction between Ras and GAP that satisfies numerous biochemical and genetic data on this important regulatory process.

  • Watanabe G et al.
  • Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho.
  • Science. 1996; 271: 645-8
  • Display abstract

  • The Rho guanosine 5'-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.

  • Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ
  • RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.
  • Nature. 1996; 383: 172-5
  • Display abstract

  • Signaling pathways using heterotrimeric guanine-nucleotide-binding-proteins (G proteins) trigger physiological responses elicited by hormones, neurotransmitters and sensory stimuli. GTP binding activates G proteins by dissociating G alpha from G beta gamma subunits, and GTP hydrolysis by G alpha subunits deactivates G proteins by allowing heterotrimers to reform. However, deactivation of G-protein signalling pathways in vivo can occur 10- to 100-fold faster than the rate of GTP hydrolysis of G alpha subunits in vitro, suggesting that GTPase-activating proteins (GAPs) deactivate G alpha subunits. Here we report that RGS (for regulator of G-protein signalling) proteins are GAPs for G alpha subunits. RGS1, RGS4 and GAIP (for G alpha-interacting protein) bind specifically and tightly to G alphai and G alpha0 in cell membranes treated with GDP and AlF4(-), and are GAPs for G alphai, G alpha0 and transducin alpha-subunits, but not for G alphas. Thus, these RGS proteins are likely to regulate a subset of the G-protein signalling pathways in mammalian cells. Our results provide insight into the mechanisms that govern the duration and specificity of physiological responses elicited by G-protein-mediated signalling pathways.

  • Zigmond SH
  • Signal transduction and actin filament organization.
  • Curr Opin Cell Biol. 1996; 8: 66-73
  • Display abstract

  • Small GTP-binding proteins of the Rho family appear to integrate extracellular signals from diverse receptor types and initiate rearrangements of F-actin. Active members of the Rho family, Rho and Rac, are now joined by Cdc42 which induces filopodia. Downstream of the Rho family proteins, actin polymerization may be induced by an increase in the availability of actin filament barbed ends. Actin organization may be affected by exposure of actin-binding sites on proteins such as vinculin and ezrin.

  • Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A
  • Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form.
  • Nature. 1995; 374: 378-81
  • Display abstract

  • The Ran proteins constitute a distinct branch of the superfamily of Ras-related GTP-binding proteins which function as molecular switches cycling between GTP-bound 'on' and GDP-bound 'off' states. Ran is located predominantly in the nucleus of eukaryotic cells and is involved in the nuclear import of proteins as well as in control of DNA synthesis and of cell-cycle progression. We report here the crystal structure at 2.3 A resolution of human Ran (Mr 24K) complexed with GDP and Mg2+. This structure reveals a similarity with the Ras core (G-domain) but with significant variations in regions involved in GDP and Mg2+ coordination (switch I and switch II regions in Ras), suggesting that there could be major conformational changes upon GTP binding. In addition to the G-domain, an extended chain and an alpha-helix were identified at the carboxy terminus. The amino-terminal (amino-acid residues MAAQGEP) stretch and the acidic tail (DEDDDL) appear to be flexible in the crystal structure.

• Disease (disease genes where sequence variants are found in this domain)

• SwissProt sequences and OMIM curated human diseases associated with missense mutations within the RHO domain.

  Protein	Disease
  Ras-related protein Rab-27A (SRS)(SMART)	OMIM:603868: Griscelli syndrome OMIM:214450:
  GTPase NRas precursor (SRS)(SMART)	OMIM:164790: Colorectal cancer
  GTPase KRas precursor (SRS)(SMART)	OMIM:190070: Colorectal adenoma ; Colorectal cancer
  Isoform 2B of P01116 (SRS)(SMART)	OMIM:190070: Colorectal adenoma ; Colorectal cancer
  Ras-related protein R-Ras2 precursor (SRS)(SMART)	OMIM:600098: ONCOGENE TC21
  GTPase HRas precursor (SRS)(SMART)	OMIM:190020: Bladder cancer OMIM:109800:

• Metabolism (metabolic pathways involving proteins which contain this domain)

• % proteins involved KEGG pathway ID Description 9.21 map04360 Axon guidance 7.77 map04670 Leukocyte transendothelial migration 7.34 map04520 Adherens junction 7.34 map04510 Focal adhesion 7.34 map04810 Regulation of actin cytoskeleton 5.76 map04370 VEGF signaling pathway 5.76 map04010 MAPK signaling pathway 5.76 map05212 Pancreatic cancer 4.46 map05210 Colorectal cancer 4.46 map04530 Tight junction 4.46 map04310 Wnt signaling pathway 4.46 map04660 T cell receptor signaling pathway 4.17 map05120 Epithelial cell signaling in Helicobacter pylori infection 4.17 map05211 Renal cell carcinoma 2.88 map04664 Fc epsilon RI signaling pathway 2.88 map04662 B cell receptor signaling pathway 2.88 map04912 GnRH signaling pathway 2.88 map04650 Natural killer cell mediated cytotoxicity 1.58 map04350 TGF-beta signaling pathway 1.29 map05030 Amyotrophic lateral sclerosis (ALS) 1.29 map04620 Toll-like receptor signaling pathway 1.01 map04120 Ubiquitin mediated proteolysis 0.86 map04910 Insulin signaling pathway This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with RHO domain which could be assigned to a KEGG orthologous group, and not all proteins containing RHO domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of RHO domains in PDB

  PDB code	Main view	Title
  1a2b		Human rhoa complexed with gtp analogue
  1a4r		G12v mutant of human placental cdc42 gtpase in the gdp form
  1aje		Cdc42 from human, nmr, 20 structures
  1am4		Complex between cdc42hs.gmppnp and p50 rhogap (h. sapiens)
  1an0		Cdc42hs-gdp complex
  1cc0		Crystal structure of the rhoa.gdp-rhogdi complex
  1cee		Solution structure of cdc42 in complex with the gtpase binding domain of wasp
  1cf4		Cdc42/ack gtpase-binding domain complex
  1cxz		Crystal structure of human rhoa complexed with the effector domain of the protein kinase pkn/prk1
  1doa		Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
  1dpf		Crystal structure of a mg-free form of rhoa complexed with gdp
  1ds6		Crystal structure of a rac-rhogdi complex
  1e0a		Cdc42 complexed with the gtpase binding domain of p21 activated kinase
  1e96		Structure of the rac/p67phox complex
  1ees		Solution structure of cdc42hs complexed with a peptide derived from p-21 activated kinase, nmr, 20 structures
  1foe		Crystal structure of rac1 in complex with the guanine nucleotide exchange region of tiam1
  1ftn		Crystal structure of the human rhoa/gdp complex
  1g4u		Crystal structure of the salmonella tyrosine phosphatase and gtpase activating protein sptp bound to rac1
  1grn		Crystal structure of the cdc42/cdc42gap/alf3 complex.
  1gwn		The crystal structure of the core domain of rhoe/rnd3- a constitutively activated small g protein
  1gzs		Crystal structure of the complex between the gef domain of the salmonella typhimurium sope toxin and human cdc42
  1he1		Crystal structure of the complex between the gap domain of the pseudomonas aeruginosa exos toxin and human rac
  1hh4		Rac1-rhogdi complex involved in nadph oxidase activation
  1i4d		Crystal structure analysis of rac1-gdp complexed with arfaptin (p21)
  1i4l		Crystal structure analysis of rac1-gdp in complex with arfaptin (p41)
  1i4t		Crystal structure analysis of rac1-gmppnp in complex with arfaptin
  1ki1		Guanine nucleotide exchange region of intersectin in complex with cdc42
  1kmq		Crystal structure of a constitutively activated rhoa mutant (q63l)
  1kz7		Crystal structure of the dh/ph fragment of murine dbs in complex with the placental isoform of human cdc42
  1kzg		Dbscdc42(y889f)
  1lb1		Crystal structure of the dbl and pleckstrin homology domains of dbs in complex with rhoa
  1m7b		Crystal structure of rnd3/rhoe: functional implications
  1mh1		Small g-protein
  1nf3		Structure of cdc42 in a complex with the gtpase-binding domain of the cell polarity protein, par6
  1ow3		Crystal structure of rhoa.gdp.mgf3-in complex with rhogap
  1ryf		Alternative splicing of rac1 generates rac1b, a self- activating gtpase
  1ryh		Alternative splicing of rac1 generates rac1b, a self- activating gtpase
  1s1c		Crystal structure of the complex between the human rhoa and rho-binding domain of human rocki
  1tx4		Rho/rhogap/gdp(dot)alf4 complex
  1x86		Crystal structure of the dh/ph domains of leukemia- associated rhogef in complex with rhoa
  1xcg		Crystal structure of human rhoa in complex with dh/ph fragment of pdzrhogef
  1z2c		Crystal structure of mdia1 gbd-fh3 in complex with rhoc- gmppnp
  2ase		Nmr structure of the f28l mutant of cdc42hs
  2atx		Crystal structure of the tc10 gppnhp complex
  2c2h		Crystal structure of the human rac3 in complex with gdp
  2cls		The crystal structure of the human rnd1 gtpase in the active gtp bound state
  2dfk		Crystal structure of the cdc42-collybistin ii complex
  2fju		Activated rac1 bound to its effector phospholipase c beta 2
  2fv8		The crystal structure of rhob in the gdp-bound state
  2g0n		The crystal structure of the human rac3 in complex with gdp and chloride
  2gcn		Crystal structure of the human rhoc-gdp complex
  2gco		Crystal structure of the human rhoc-gppnhp complex
  2gcp		Crystal structure of the human rhoc-gsp complex
  2h7v		Co-crystal structure of ypka-rac1
  2ic5		Crystal structure of human rac3 grown in the presence of gpp(nh)p.
  2j0v		The crystal structure of arabidopsis thaliana rac7-rop9: the first ras superfamily gtpase from the plant kingdom
  2j1l		Crystal structure of human rho-related gtp-binding protein rhod
  2ngr		Transition state complex for gtp hydrolysis by cdc42: comparisons of the high resolution structures for cdc42 bound to the active and catalytically compromised forms of the cdc42-gap.
  2nty		Rop4-gdp-prone8
  2nz8		N-terminal dhph cassette of trio in complex with nucleotide- free rac1
  2odb		The crystal structure of human cdc42 in complex with the crib domain of human p21-activated kinase 6 (pak6)
  2ov2		The crystal structure of the human rac3 in complex with the crib domain of human p21-activated kinase 4 (pak4)
  2p2l		Rac1-gdp-zinc complex
  2q3h		The crystal structure of rhoua in the gdp-bound state.
  2qme		Crystal structure of human rac3 in complex with crib domain of human p21-activated kinase 1 (pak1)
  2qrz		Cdc42 bound to gmp-pcp: induced fit by effector is required
  2rex		Crystal structure of the effector domain of plxnb1 bound with rnd1 gtpase
  2rgn		Crystal structure of p63rhogef complex with galpha-q and rhoa
  2rmk		Rac1/prk1 complex
  2v55
  2vrw		Critical structural role for the ph and c1 domains of the vav1 exchange factor
  2w2t
  2w2v
  2w2x
  2wbl
  2wkp
  2wkq
  2wkr
  2wm9
  2wmn
  2wmo
  3bji		Structural basis of promiscuous guanine nucleotide exchange by the t-cell essential vav1
  3bwd		Crystal structure of the plant rho protein rop5
  3eg5
  3gcg

• Links (links to other resources describing this domain)

• INTERPRO	IPR003578